Salicylic Acid Signaling Controls the Maturation and Localization of the Arabiclopsis Defense Protein ACCELERATED CELL DEATH6

ACCELERATED CELL DEATH6 （ACD6） is a multipass membrane protein with an ankyrin domain that acts in a positive feedback loop with the defense signal salicylic acid （SA）. This study implemented biochemical approaches to infer changes in ACD6 complexes and localization. In addition to forming endoplasmic reticulum （ER）- and plasma membrane （PM）-Iocalized complexes, ACD6 forms soluble complexes, where it is bound to cytosolic HSP70, ubiquitinated, and degraded via the proteasome. Thus, ACD6 constitutively undergoes ER-associated degradation. During SA signaling, the soluble ACD6 pool decreases, whereas the PM pool increases. Similarly, ACD6-1, an activated version of ACD6 that induces SA, is present at low levels in the soluble fraction and high levels in the PM. However, ACD6 variants with amino acid substitutions in the ankyrin domain form aberrant, inactive complexes, are induced by a SA agonist, but show no PM localization. SA signaling also increases the PM pools of FLAGELLIN SENSING2 （FLS2） and BRI1-ASSOClATED RECEPTOR KINASE 1 （BAK1）. FLS2 forms complexes ACD6; both FLS2 and BAK1 require ACD6 for maximal accumulation at the PM in response to SA signaling. A plausible scenario is that SA increases the efficiency of productive folding and/or complex formation in the ER, such that ACD6, together with FLS2 and BAK1, reaches the cell surface to more effectively promote immune responses.     

安徽将建世界最大抗体药物基地

<正>近日,安徽合肥半汤生物经济实验区重大合作项目集中签约仪式在合肥举行,35个国际、国内合作项目集中签约,包括抗癌药物等多种抗体药未来将实现本地化生产。来自美国的BioA tla有限公司将和北大未名合作研发"第四代抗体技术",意味着我国的肿瘤患者未来将使用上便宜而有效的抗癌药物。合肥半汤生物经济实验区     

序列同源性比较软件Blast的本地化实现及VB接口程序的编制

美国国家生物技术信息中心（ＮａｔｉｏｎａｌＣｅｎｔｅｒｆｏｒＢｉｏｔｅｃｈｎｏｌｏｇｙＩｎｆｏｒｍａｔｉｏｎ,ＮＣＢＩ）的Ｂｌａｓｔ软件是进行核酸序列和蛋白质序列同源性比较的有力工具［１,２］．通过访问ＮＣＢＩ的主页（ｈｔｔｐ：／／ｗｗｗ．ｎｃｂｉ．ｎｌｍ．ｎｉｈ．ｇｏｖ）进行Ｂｌａｓｔ同源性比较是常用的分析方法．然而在很多场合需要在脱机状态下使用Ｂｌａｓｔ进行同源性比较,所以,Ｂｌａｓｔ软件的本地化实现有其必要性．本文介绍实现Ｂｌａｓｔ本地化过程的经验,同时用ＶｉｓｕａｌＢａｓｉｃ５．０（以下…     

B23 interacts with PES1 and is involved in nucleolar localization of PES1

PES1, the human homolog of zebrafish pescadillo, is a nucleolar protein that is essential for cell proliferation. We report herein that a nucleolar marker protein B23 physically interacts with PES1 and is involved in the nucleolar localization of PES1. In vivo interaction between B23 and PES1 was verified by co-immunopreci- pitation of endogenous B23 and PES1 proteins, and they showed cellular co-localizations under both normal and actinomycin D-induced stress conditions. Furthermore, we mapped their interaction domains via in vitro pull- down assays. When B23 was knocked down by RNA interference, there appeared an increased nucleoplasmic distribution of PES1. Our results support a previous hypothesis that B23 might be a nucleolar hub protein for protein targeting to the nucleolus, and shed light on the nucleolar localization mechanism of PESI. The physical interaction between B23 and PES1 implies that they may participate in ribosome biogenesis in a protein complex.     

Localization and functional analysis of SeMNPV IE1 in mammalian cells

In this paper, the function of the iel gene from baculovirus Spodoptera exigua multiple nucleopolyhedrovirus (SeMNPV), belonging to group Ⅱ nucleopolyhedrovirus, was studied in mammalian cells.We amplified the SeMNPV ie1 gene and expressed it by fusing to the C terminal of enhanced GFP protein in HEK 293 cells. Confocal microscopy revealed that the IE1-GFP fusion protein was localized in the nucleus of the mammalian cells. The promoter sequences of AcMNPV gp64, SeMNPV F protein and Drosophila hsp70 were also analyzed, to further study the function of SeMNPV IE1. The results showed that, in the absence of the hr sequence, IE1 improved the expression of the F promoter but didn't influence the gp64 promoter significantly, but IE1 moderately stimulated the hsp70 promoter.     

The Rice Restorer Rf4 for Wild-Abortive Cytoplasmic Male Sterility Encodes a MitochondriaI-Localized PPR Protein that Functions in Reduction of WA352Transcripts

Dear Editor, Cytoplasmic male sterility （CMS）, the failure to produce functional male gametes, is widespread in flowering plants （Kaul, 1988）. Nuclear Restoration of Fertility （Rf） genes can make CMS lines fertile; thus, CMS provides both an ideal model system to study the interaction between mitochondrial and nuclear genomes, and a useful genetic tool for breeding to exploit hybrid vigor in crops （reviewed in Chen and Liu, 2014）. Hybrid rice, with -20%-30% higher yields, has been successfully developed with a three-line （CMS, maintainer, and restorer） system, and released for large-scale production in China in the 1970s （Lin and Yuan, 1980）. This major achievement in agriculture results mainly from the discovery and use of the Wild-Abortive type CMS （CMS-WA） cytoplasm from the wild rice （Oryza rufipogon Griff.） and its Rf genes in indica rice （0. sativa L. ssp. indica） cultivars （Lin and Yuan, 1980）.     

Phosphatidic Acid （PA） PP2A Activity and PIN1 Binds PP2AA1 to Regulate Polar Localization

Phospholipase D （PLD） exerts broad biological functions in eukaryotes through regulating downstream effectors by its product, phosphatidic acid （PA）. Protein kinases and phosphatases, such as mammalian target of rapa- mycin （mTOR）, Protein Phosphatase 1 （PP1） and Protein Phosphatase 2C （PP2C）, are PA-binding proteins that execute crucial regulatory functions in both animals and plants. PA participates in many signaling pathways by modulating the enzymatic activity and/or subcellular localization of bound proteins. In this study, we demonstrated that PLD-derived PA interacts with the scaffolding A1 subunit of Protein Phosphatase 2A （PP2A） and regulates PP2A-mediated PIN1 dephos- phorylation in Arabidopsis. Genetic and pharmacological studies showed that both PA and PP2A participate in the regu- lation of auxin distribution. In addition, both the phosphorylation status and polar localization of PIN1 protein were affected by PLD inhibitors, Exogenous PA triggered the membrane accumulation of PP2AA1 and enhanced the PP2A activity at membrane, while PLD inhibition resulted in the reduced endosomal localization and perinuclear aggregation of PP2AA1. These results demonstrate the important role of PLD-derived PA in normal PP2A-mediated PIN dephosphoryl- ation and reveal a novel mechanism, in which PA recruits PP2AA1 to the membrane system and regulates PP2A function on membrane-targeted proteins. As PA and PP2A are conserved among eukaryotes, other organisms might use similar mechanisms to mediate multiple biological processes.